SPG7_MOUSE
ID SPG7_MOUSE Reviewed; 781 AA.
AC Q3ULF4; B2RQY8; D3Z1Z1; Q4V9T9; Q7TNG0; Q80X42; Q811Y5; Q8K414; Q8R1A1;
AC Q8R1K2;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Paraplegin {ECO:0000303|PubMed:14722615};
DE EC=3.4.24.-;
DE AltName: Full=Spastic paraplegia 7 protein {ECO:0000312|MGI:MGI:2385906};
DE Flags: Precursor;
GN Name=Spg7 {ECO:0000312|MGI:MGI:2385906};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND DISRUPTION PHENOTYPE.
RC STRAIN=Swiss Webster / NIH;
RX PubMed=14722615; DOI=10.1172/jci200420138;
RA Ferreirinha F., Quattrini A., Pirozzi M., Valsecchi V., Dina G.,
RA Broccoli V., Auricchio A., Piemonte F., Tozzi G., Gaeta L., Casari G.,
RA Ballabio A., Rugarli E.I.;
RT "Axonal degeneration in paraplegin-deficient mice is associated with
RT abnormal mitochondria and impairment of axonal transport.";
RL J. Clin. Invest. 113:231-242(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ;
RA Ungaro P., Milano A., Cocozza S.;
RT "Cloning and expression analysis of the mouse Spg7 cDNA.";
RL Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II, and FVB/N; TISSUE=Brain, Kidney, Liver, and Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [6]
RP PROTEIN SEQUENCE OF 44-53 AND 106-115, PROTEOLYTIC PROCESSING, SUBUNIT,
RP INTERACTION WITH AFG3L1 AND AFG3L2, MUTAGENESIS OF GLU-575, AND SUBCELLULAR
RP LOCATION.
RX PubMed=19656850; DOI=10.1091/mbc.e09-03-0218;
RA Koppen M., Bonn F., Ehses S., Langer T.;
RT "Autocatalytic processing of m-AAA protease subunits in mitochondria.";
RL Mol. Biol. Cell 20:4216-4224(2009).
RN [7]
RP NITRATION [LARGE SCALE ANALYSIS] AT TYR-505, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16800626; DOI=10.1021/bi060474w;
RA Sacksteder C.A., Qian W.-J., Knyushko T.V., Wang H., Chin M.H., Lacan G.,
RA Melega W.P., Camp D.G. II, Smith R.D., Smith D.J., Squier T.C.,
RA Bigelow D.J.;
RT "Endogenously nitrated proteins in mouse brain: links to neurodegenerative
RT disease.";
RL Biochemistry 45:8009-8022(2006).
RN [8]
RP SUBUNIT.
RX PubMed=17101804; DOI=10.1128/mcb.01470-06;
RA Koppen M., Metodiev M.D., Casari G., Rugarli E.I., Langer T.;
RT "Variable and tissue-specific subunit composition of mitochondrial m-AAA
RT protease complexes linked to hereditary spastic paraplegia.";
RL Mol. Cell. Biol. 27:758-767(2007).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [10]
RP SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH AFG3L2,
RP AND CAUTION.
RX PubMed=22563492; DOI=10.1371/journal.pone.0036337;
RA Mancuso G., Barth E., Crivello P., Rugarli E.I.;
RT "Alternative splicing of Spg7, a gene involved in hereditary spastic
RT paraplegia, encodes a variant of paraplegin targeted to the endoplasmic
RT reticulum.";
RL PLoS ONE 7:E36337-E36337(2012).
CC -!- FUNCTION: ATP-dependent zinc metalloprotease. Plays a role in the
CC formation and regulation of the mitochondrial permeability transition
CC pore (mPTP) and its proteolytic activity is dispensable for this
CC function (By similarity). {ECO:0000250|UniProtKB:Q9UQ90, ECO:0000305}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q9WZ49};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:Q9WZ49};
CC -!- SUBUNIT: Forms heterooligomers with AFG3L1 and AFG3L2 (PubMed:22563492,
CC PubMed:17101804, PubMed:19656850). Component of the mitochondrial
CC permeability transition pore complex (mPTPC), at least composed of
CC SPG7, VDAC1 and PPIF (By similarity). Interacts with AFG3L2; the
CC interaction is required for the efficient assembly of mitochondrial
CC complex I (PubMed:22563492, PubMed:19656850). Interacts with AFG3L1
CC (PubMed:19656850). Interacts with MAIP1. Interacts with VDAC1 and PPIF
CC (By similarity). {ECO:0000250|UniProtKB:Q9UQ90,
CC ECO:0000269|PubMed:17101804, ECO:0000269|PubMed:19656850,
CC ECO:0000269|PubMed:22563492}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:19656850, ECO:0000269|PubMed:22563492}; Multi-pass
CC membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in the brain and retina (at protein
CC level). {ECO:0000269|PubMed:22563492}.
CC -!- PTM: Upon import into the mitochondrion, the N-terminal transit peptide
CC is cleaved by the mitochondrial-processing peptidase (MPP) to generate
CC an intermediate form which undergoes a second proteolytic cleavage
CC mediated by proteases AFG3L1 and/or AFG3L2 removing an additional N-
CC terminal fragment to generate the proteolytically active mature form.
CC {ECO:0000269|PubMed:19656850}.
CC -!- DISRUPTION PHENOTYPE: Mice are affected by a distal axonopathy of
CC spinal and peripheral axons, characterized by axonal swelling and
CC degeneration. Mitochondrial morphological abnormalities occur in
CC synaptic terminals and in distal regions of axons long before the first
CC signs of swelling and degeneration and correlate with onset of motor
CC impairment during a rotarod test. {ECO:0000269|PubMed:14722615}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the AAA ATPase
CC family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the peptidase M41
CC family. {ECO:0000305}.
CC -!- CAUTION: According to PubMed:22563492, alternative splicing gives rise
CC to an isoform (Paraplegin-2) which is identical to the sequence of the
CC mature protein and localizes to the endoplasmic reticulum.
CC {ECO:0000305|PubMed:19656850}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH55488.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH96690.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF512565; AAN03852.1; -; mRNA.
DR EMBL; AF547215; AAO21098.1; -; mRNA.
DR EMBL; AK145540; BAE26494.1; -; mRNA.
DR EMBL; AC121819; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC024466; AAH24466.1; -; mRNA.
DR EMBL; BC024986; AAH24986.1; -; mRNA.
DR EMBL; BC051051; AAH51051.1; -; mRNA.
DR EMBL; BC096690; AAH96690.1; ALT_INIT; mRNA.
DR EMBL; BC055488; AAH55488.1; ALT_INIT; mRNA.
DR EMBL; BC138141; AAI38142.1; -; mRNA.
DR CCDS; CCDS40508.1; -.
DR RefSeq; NP_694816.3; NM_153176.4.
DR AlphaFoldDB; Q3ULF4; -.
DR SMR; Q3ULF4; -.
DR BioGRID; 231586; 3.
DR STRING; 10090.ENSMUSP00000119552; -.
DR MEROPS; M41.006; -.
DR iPTMnet; Q3ULF4; -.
DR PhosphoSitePlus; Q3ULF4; -.
DR EPD; Q3ULF4; -.
DR MaxQB; Q3ULF4; -.
DR PaxDb; Q3ULF4; -.
DR PRIDE; Q3ULF4; -.
DR ProteomicsDB; 261134; -.
DR Antibodypedia; 30863; 406 antibodies from 21 providers.
DR DNASU; 234847; -.
DR Ensembl; ENSMUST00000149248; ENSMUSP00000119552; ENSMUSG00000000738.
DR GeneID; 234847; -.
DR KEGG; mmu:234847; -.
DR UCSC; uc009nuc.1; mouse.
DR CTD; 6687; -.
DR MGI; MGI:2385906; Spg7.
DR VEuPathDB; HostDB:ENSMUSG00000000738; -.
DR eggNOG; KOG0731; Eukaryota.
DR GeneTree; ENSGT00940000156329; -.
DR InParanoid; Q3ULF4; -.
DR OMA; TRMKSMK; -.
DR OrthoDB; 217929at2759; -.
DR TreeFam; TF105003; -.
DR BRENDA; 3.4.24.B18; 3474.
DR Reactome; R-MMU-8949664; Processing of SMDT1.
DR BioGRID-ORCS; 234847; 0 hits in 75 CRISPR screens.
DR ChiTaRS; Spg7; mouse.
DR PRO; PR:Q3ULF4; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q3ULF4; protein.
DR Bgee; ENSMUSG00000000738; Expressed in retinal neural layer and 199 other tissues.
DR ExpressionAtlas; Q3ULF4; baseline and differential.
DR Genevisible; Q3ULF4; MM.
DR GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR GO; GO:0005745; C:m-AAA complex; IDA:MGI.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:UniProtKB.
DR GO; GO:0005757; C:mitochondrial permeability transition pore complex; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0004176; F:ATP-dependent peptidase activity; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:Ensembl.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0008089; P:anterograde axonal transport; IMP:MGI.
DR GO; GO:0007155; P:cell adhesion; TAS:MGI.
DR GO; GO:1902686; P:mitochondrial outer membrane permeabilization involved in programmed cell death; ISS:UniProtKB.
DR GO; GO:0034982; P:mitochondrial protein processing; IBA:GO_Central.
DR GO; GO:0007005; P:mitochondrion organization; IMP:MGI.
DR GO; GO:0065003; P:protein-containing complex assembly; IBA:GO_Central.
DR GO; GO:0030155; P:regulation of cell adhesion; TAS:MGI.
DR GO; GO:0046902; P:regulation of mitochondrial membrane permeability; ISS:UniProtKB.
DR Gene3D; 1.20.58.760; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_01458; FtsH; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041569; AAA_lid_3.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR005936; FtsH.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR011546; Pept_M41_FtsH_extracell.
DR InterPro; IPR000642; Peptidase_M41.
DR InterPro; IPR037219; Peptidase_M41-like.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF17862; AAA_lid_3; 1.
DR Pfam; PF06480; FtsH_ext; 1.
DR Pfam; PF01434; Peptidase_M41; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF140990; SSF140990; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR01241; FtsH_fam; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Direct protein sequencing; Hydrolase; Membrane; Metal-binding;
KW Metalloprotease; Mitochondrion; Mitochondrion inner membrane; Nitration;
KW Nucleotide-binding; Protease; Reference proteome; Transit peptide;
KW Transmembrane; Transmembrane helix; Zinc.
FT TRANSIT 1..43
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:19656850"
FT PROPEP 44..105
FT /note="Removed in mature form"
FT /evidence="ECO:0000305|PubMed:19656850"
FT /id="PRO_0000442306"
FT CHAIN 106..781
FT /note="Paraplegin"
FT /id="PRO_0000442307"
FT TOPO_DOM 106..144
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000305"
FT TRANSMEM 145..165
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 166..248
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000305"
FT TRANSMEM 249..269
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 270..781
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000305"
FT REGION 22..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 103..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 701..781
FT /note="Interaction with PPIF"
FT /evidence="ECO:0000250|UniProtKB:Q9UQ90"
FT COMPBIAS 107..135
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 575
FT /evidence="ECO:0000250|UniProtKB:Q9WZ49"
FT BINDING 312
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9UQ90"
FT BINDING 349..357
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9UQ90"
FT BINDING 492
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9UQ90"
FT BINDING 574
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9WZ49"
FT BINDING 578
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9WZ49"
FT BINDING 650
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9WZ49"
FT MOD_RES 505
FT /note="3'-nitrotyrosine"
FT /evidence="ECO:0007744|PubMed:16800626"
FT MUTAGEN 575
FT /note="E->Q: Absence of proteolytic activity. No loss of
FT its processing into the mature form."
FT /evidence="ECO:0000269|PubMed:19656850"
FT CONFLICT 165
FT /note="I -> T (in Ref. 2; AAO21098)"
FT /evidence="ECO:0000305"
FT CONFLICT 168
FT /note="A -> S (in Ref. 5; AAI38142)"
FT /evidence="ECO:0000305"
FT CONFLICT 310
FT /note="D -> G (in Ref. 2; AAO21098)"
FT /evidence="ECO:0000305"
FT CONFLICT 471
FT /note="L -> F (in Ref. 1; AAN03852)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 781 AA; 85996 MW; 35CCFB8F24B249D8 CRC64;
MAAALLLLRG LRPGPEPRPR RLWGLLSGRG PGLSSGAGAR RPYAARGTPV GPAAAGGHAP
QSLLLRILTP SFEGISGLLL KQHIVPNAVR LWPLSGSTLY FNTSRMKQKN KDNDKPKGKT
PEDDEEEKRR KEREDQMYRE RLRTLFIIAL VMSLLNSLST SGGSISWADF VNEMLAKGEV
QRVQVVPESD VVEVYLHPGA VVFGRPRLAL MYRMQVANID KFEEKLRAAE DELNIESKDR
IPVSYKRTGF FGNALYALGM TAVGLAILWY VFRLAGMTGR EGGFSAFNQL KMARFTIVDG
KTGKGVSFQD VAGMHEAKLE VREFVDYLKS PERFLQLGAK VPKGALLLGP PGCGKTLLAK
AVATEAQVPF LAMAGPEFVE VIGGLGAARV RSLFKEARAR APCIVYIDEI DAVGKKRSTS
MSGFSNTEEE QTLNQLLVEM DGMGTTDHVI VLASTNRADV LDNALMRPGR LDRHVFIDLP
TLQERREIFE QHLKGLKLTQ PSSFYSQRLA ELTPGFSGAD IANICNEAAL HAAREGHTSV
HTFNFEYAVE RVIAGTAKKS KILSKEEQRV VAFHESGHAL VGWLLEHTEA VMKVSIAPRT
NAALGFSQML PRDQYLFTKE QLFERMCMAL GGRAAEAISF SRVTSGAQDD LRKVTRIAYS
MVKQFGMAPS IGPVSFPEAQ EGLMGIGRRP FSQGLQQMMD HEAKLLVAKA YRHTEKVLLD
NLDKLQALAN ALLEKEVINY EDIEALIGPP PHGPKKMIAP QKWIDAEKER QASGEEEAPA
P
